+Open data
-Basic information
Entry | Database: PDB / ID: 1rkl | ||||||
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Title | NMR structure of yeast oligosaccharyltransferase subunit Ost4p | ||||||
Components | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 4 kDa subunit | ||||||
Keywords | TRANSFERASE / membrane protein | ||||||
Function / homology | Oligosaccaryltransferase / Oligosaccharyltransferase subunit ost4p superfamily / Oligosaccaryltransferase / oligosaccharyltransferase complex / protein N-linked glycosylation / protein-macromolecule adaptor activity / endoplasmic reticulum membrane / mitochondrion / Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4 Function and homology information | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Zubkov, S. / Lennarz, W.J. / Mohanty, S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase Authors: Zubkov, S. / Lennarz, W.J. / Mohanty, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rkl.cif.gz | 219.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rkl.ent.gz | 177.5 KB | Display | PDB format |
PDBx/mmJSON format | 1rkl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rkl_validation.pdf.gz | 352.5 KB | Display | wwPDB validaton report |
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Full document | 1rkl_full_validation.pdf.gz | 471.1 KB | Display | |
Data in XML | 1rkl_validation.xml.gz | 21.4 KB | Display | |
Data in CIF | 1rkl_validation.cif.gz | 32.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rk/1rkl ftp://data.pdbj.org/pub/pdb/validation_reports/rk/1rkl | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3986.696 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide occurs naturally in Saccharomyces cerevisiae (yeast). References: UniProt: Q99380, EC: 2.4.1.119 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 1mM Ost4p / Solvent system: 4:4:1 CDCl3:CD3OD:D2O | ||||||||||||
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: 287 NOE restraints, 58 dihedral angle restraints, 24 distance restraints from hydrogen bonds | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 |